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8VTM

Crystal structure of R. sphaeroides Photosynthetic Reaction Center variant Y(M210)2-bromophenylalanine

8VTM の概要
エントリーDOI10.2210/pdb8vtm/pdb
分子名称Reaction center protein H chain, CARDIOLIPIN, Reaction center protein L chain, ... (11 entities in total)
機能のキーワードphotosynthesis, membrane protein, electron transfer
由来する生物種Cereibacter sphaeroides
詳細
タンパク質・核酸の鎖数3
化学式量合計99382.83
構造登録者
Tran, K.,Mathews, I.,Boxer, S.G. (登録日: 2024-01-26, 公開日: 2024-03-13, 最終更新日: 2025-09-24)
主引用文献Tran, K.N.,Faries, K.M.,Magdaong, N.C.M.,Mathews, I.I.,Weaver, J.B.,Kirsh, J.M.,Holten, D.,Kirmaier, C.,Boxer, S.G.
Application of Amber Suppression To Study the Role of Tyr M210 in Electron Transfer in Rhodobacter sphaeroides Photosynthetic Reaction Centers.
J.Phys.Chem.B, 129:3317-3333, 2025
Cited by
PubMed Abstract: The initial light-induced electron transfer (ET) steps in the bacterial photosynthetic reaction center (RC) have been extensively studied and provide a paradigm for connecting structure and function. Although RCs have local pseudo- symmetry, ET only occurs along the A branch of chromophores. Tyrosine M210 is a key symmetry-breaking residue adjacent to bacteriochlorophyll B that bridges the primary electron donor P and the bacteriopheophytin acceptor H. We used amber suppression to incorporate phenylalanine variants with different electron-withdrawing/-donating capabilities at the position M210. X-ray data generally reveal no appreciable structural changes due to the mutations. P* decay and PH formation are multiexponential (∼2 to 9, ∼10 to 60, and ∼100 to 300 ps) and temperature dependent. The 1020 nm transient-absorption band of PB is barely resolved for a few variants at 295 K and for none at 77 K. The results indicate a change from two-step ET for wild-type RCs to the dominance of one-step superexchange ET for the mutants. Resonance Stark spectroscopy reveals that the free energy of PB changes by -57 to +66 meV among the phenylalanine variants. Because PB apparently lies above P* in all phenylalanine variants, the perturbations primarily affect the energy denominator for superexchange mixing. The findings deepen insight into primary ET in the bacterial RC.
PubMed: 40134359
DOI: 10.1021/acs.jpcb.5c00082
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.51 Å)
構造検証レポート
Validation report summary of 8vtm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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